STAB2_HUMAN
ID STAB2_HUMAN Reviewed; 2551 AA.
AC Q8WWQ8; Q6ZMK2; Q7Z5N9; Q86UR4; Q8IUG9; Q8TES1; Q9H7H7; Q9NRY3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Stabilin-2;
DE AltName: Full=FAS1 EGF-like and X-link domain-containing adhesion molecule 2;
DE AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2;
DE Short=FEEL-2;
DE AltName: Full=Hyaluronan receptor for endocytosis;
DE Contains:
DE RecName: Full=190 kDa form stabilin-2;
DE AltName: Full=190 kDa hyaluronan receptor for endocytosis;
DE Flags: Precursor;
GN Name=STAB2 {ECO:0000312|EMBL:CAC82105.1};
GN Synonyms=FEEL2 {ECO:0000303|PubMed:12077138}, FELL {ECO:0000303|Ref.7},
GN FEX2 {ECO:0000303|Ref.3}, HARE {ECO:0000312|EMBL:AAO39681.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:CAC82105.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT HIS-510.
RX PubMed=11829752; DOI=10.1042/0264-6021:3620155;
RA Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P.,
RA Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J.,
RA Longati P., Velten F.W., Johansson S., Goerdt S.;
RT "Stabilin-1 and -2 constitute a novel family of fasciclin-like hyaluronan
RT receptor homologues.";
RL Biochem. J. 362:155-164(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC15608.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP HIS-510.
RX PubMed=12077138; DOI=10.1074/jbc.m204277200;
RA Adachi H., Tsujimoto M.;
RT "FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and
RT angiogenesis-modulating activities.";
RL J. Biol. Chem. 277:34264-34270(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAP74958.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Park S.-Y., Kim I.-S.;
RT "FEX2, a novel cell adhesion molecule of Fas-1 superfamily mediates cell-
RT cell interaction.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB15793.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, AND VARIANT THR-2039.
RC TISSUE=Spleen {ECO:0000312|EMBL:BAB15793.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAP74958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, AND VARIANTS THR-2039
RP AND VAL-2401.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAO39681.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1136-2551, PROTEIN SEQUENCE OF 1136-1144;
RP 1257-1269; 1597-1605; 1623-1645; 1652-1660; 1813-1817; 1834-1843;
RP 1914-1918; 1953-1957; 2204-2217; 2211-2215 AND 2355-2367, AND TISSUE
RP SPECIFICITY.
RX PubMed=12626425; DOI=10.1093/glycob/cwg029;
RA Zhou B., McGary C.T., Weigel J.A., Saxena A., Weigel P.H.;
RT "Purification and molecular identification of the human hyaluronan receptor
RT for endocytosis.";
RL Glycobiology 13:339-349(2003).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAP74958.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1599-2551, AND VARIANT VAL-2401.
RA Tao Q., Zhang W., Cao X.;
RT "Molecular cloning and characterization of human FELL sharing homology with
RT CD44.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 1136-1144, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=17145755; DOI=10.1074/jbc.m607787200;
RA Harris E.N., Kyosseva S.V., Weigel J.A., Weigel P.H.;
RT "Expression, processing, and glycosaminoglycan binding activity of the
RT recombinant human 315-kDa hyaluronic acid receptor for endocytosis
RT (HARE).";
RL J. Biol. Chem. 282:2785-2797(2007).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12473645; DOI=10.1074/jbc.m210211200;
RA Tamura Y., Adachi H., Osuga J., Ohashi K., Yahagi N., Sekiya M.,
RA Okazaki H., Tomita S., Iizuka Y., Shimano H., Nagai R., Kimura S.,
RA Tsujimoto M., Ishibashi S.;
RT "FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end
RT products.";
RL J. Biol. Chem. 278:12613-12617(2003).
RN [10]
RP FUNCTION.
RX PubMed=15208308; DOI=10.1074/jbc.m405322200;
RA Harris E.N., Weigel J.A., Weigel P.H.;
RT "Endocytic function, glycosaminoglycan specificity, and antibody
RT sensitivity of the recombinant human 190-kDa hyaluronan receptor for
RT endocytosis (HARE).";
RL J. Biol. Chem. 279:36201-36209(2004).
RN [11]
RP FUNCTION.
RX PubMed=15572036; DOI=10.1016/j.yexcr.2004.09.017;
RA Hansen B., Longati P., Elvevold K., Nedredal G.-I., Schledzewski K.,
RA Olsen R., Falkowski M., Kzhyshkowska J., Carlsson F., Johansson S.,
RA Smedsroed B., Goerdt S., Johansson S., McCourt P.;
RT "Stabilin-1 and stabilin-2 are both directed into the early endocytic
RT pathway in hepatic sinusoidal endothelium via interactions with
RT clathrin/AP-2, independent of ligand binding.";
RL Exp. Cell Res. 303:160-173(2005).
RN [12]
RP SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ALPHA-M/BETA-2 [ITGAM/ITGB2] INTEGRIN.
RX PubMed=17675564; DOI=10.1189/jlb.0107052;
RA Jung M.Y., Park S.Y., Kim I.S.;
RT "Stabilin-2 is involved in lymphocyte adhesion to the hepatic sinusoidal
RT endothelium via the interaction with alphaMbeta2 integrin.";
RL J. Leukoc. Biol. 82:1156-1165(2007).
RN [13]
RP ERRATUM OF PUBMED:17675564.
RA Jung M.Y., Park S.Y., Kim I.S.;
RL J. Leukoc. Biol. 83:438-438(2008).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17962816; DOI=10.1038/sj.cdd.4402242;
RA Park S.Y., Jung M.Y., Kim H.J., Lee S.J., Kim S.Y., Lee B.H., Kwon T.H.,
RA Park R.W., Kim I.S.;
RT "Rapid cell corpse clearance by stabilin-2, a membrane phosphatidylserine
RT receptor.";
RL Cell Death Differ. 15:192-201(2008).
RN [15]
RP INTERACTION WITH TMSB4X.
RX PubMed=18519035; DOI=10.1016/j.febslet.2008.03.058;
RA Lee S.J., So I.S., Park S.Y., Kim I.S.;
RT "Thymosin beta4 is involved in stabilin-2-mediated apoptotic cell
RT engulfment.";
RL FEBS Lett. 582:2161-2166(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH GULP1.
RX PubMed=18230608; DOI=10.1074/jbc.m709105200;
RA Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.;
RT "Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse
RT engulfment.";
RL J. Biol. Chem. 283:10593-10600(2008).
RN [17]
RP FUNCTION.
RX PubMed=18434317; DOI=10.1074/jbc.m710360200;
RA Harris E.N., Weigel J.A., Weigel P.H.;
RT "The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a
RT systemic clearance receptor for heparin.";
RL J. Biol. Chem. 283:17341-17350(2008).
RN [18]
RP FUNCTION.
RX PubMed=18573870; DOI=10.1128/mcb.01993-07;
RA Park S.-Y., Kim S.-Y., Jung M.-Y., Bae D.-J., Kim I.-S.;
RT "Epidermal growth factor-like domain repeat of stabilin-2 recognizes
RT phosphatidylserine during cell corpse clearance.";
RL Mol. Cell. Biol. 28:5288-5298(2008).
RN [19]
RP FUNCTION.
RX PubMed=19359419; DOI=10.1152/ajpgi.90717.2008;
RA Harris E.N., Baggenstoss B.A., Weigel P.H.;
RT "Rat and human HARE/stabilin-2 are clearance receptors for high- and low-
RT molecular-weight heparins.";
RL Am. J. Physiol. 296:G1191-G1199(2009).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1743.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2497, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Phosphatidylserine receptor that enhances the engulfment of
CC apoptotic cells. Hyaluronan receptor that binds to and mediates
CC endocytosis of hyaluronic acid (HA). Acts also, in different species,
CC as a primary systemic scavenger receptor for heparin (Hep), chondroitin
CC sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG),
CC acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides
CC and advanced glycation end products (AGE). May serve to maintain tissue
CC integrity by supporting extracellular matrix turnover or it may
CC contribute to maintaining fluidity of bodily liquids by resorption of
CC hyaluronan. Counter receptor which plays an important role in
CC lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-
CC positive and Gram-negative bacteria and may play a role in defense
CC against bacterial infection. The proteolytically processed 190 kDa form
CC also functions as an endocytosis receptor for heparin internalization
CC as well as HA and CS. {ECO:0000269|PubMed:12077138,
CC ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:15208308,
CC ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:17145755,
CC ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:17962816,
CC ECO:0000269|PubMed:18230608, ECO:0000269|PubMed:18434317,
CC ECO:0000269|PubMed:18573870, ECO:0000269|PubMed:19359419}.
CC -!- SUBUNIT: Interacts with GULP1 and heparin. Also interacts with alpha-
CC M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4 (TMSB4X and/or
CC TMSB4Y). {ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:18230608,
CC ECO:0000269|PubMed:18519035}.
CC -!- INTERACTION:
CC Q8WWQ8; P20065: Tmsb4x; Xeno; NbExp=3; IntAct=EBI-7945957, EBI-7946048;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17675564};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17675564}.
CC Cytoplasm {ECO:0000269|PubMed:17145755}. Note=Only a small amount
CC appears to be present at the cell surface (PubMed:17145755).
CC -!- TISSUE SPECIFICITY: Highly expressed in sinusoidal endothelial cells of
CC liver, spleen and lymph nodes. Also expressed in non SEC-cells such as
CC HMDMs (monocyte-derivedmacrophages), HAMs (T-cell leukemia virus type
CC 1-associated myelopathy), and several macrophage cell line.
CC {ECO:0000269|PubMed:11829752, ECO:0000269|PubMed:12077138,
CC ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:12626425,
CC ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:17962816}.
CC -!- DOMAIN: Recognizes phosphatidyl serine via its epidermal growth factor-
CC like domains.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17145755,
CC ECO:0000269|PubMed:19159218}.
CC -!- PTM: Proteolytically processed to yield a 190 kDa protein.
CC {ECO:0000269|PubMed:12626425}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82398.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD18723.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ295695; CAC82105.1; -; mRNA.
DR EMBL; AB052958; BAC15608.1; -; mRNA.
DR EMBL; AY311388; AAP74958.1; -; mRNA.
DR EMBL; AK024503; BAB15793.1; -; mRNA.
DR EMBL; AK074051; BAB84877.1; -; mRNA.
DR EMBL; AK160380; BAD18723.1; ALT_FRAME; mRNA.
DR EMBL; AY227444; AAO39681.1; -; mRNA.
DR EMBL; AF160476; AAF82398.1; ALT_INIT; mRNA.
DR CCDS; CCDS31888.1; -.
DR RefSeq; NP_060034.9; NM_017564.9.
DR PDB; 5N86; X-ray; 1.48 A; A/B=2311-2449.
DR PDBsum; 5N86; -.
DR AlphaFoldDB; Q8WWQ8; -.
DR SMR; Q8WWQ8; -.
DR BioGRID; 120727; 7.
DR IntAct; Q8WWQ8; 4.
DR MINT; Q8WWQ8; -.
DR STRING; 9606.ENSP00000373539; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR CarbonylDB; Q8WWQ8; -.
DR GlyGen; Q8WWQ8; 28 sites.
DR iPTMnet; Q8WWQ8; -.
DR PhosphoSitePlus; Q8WWQ8; -.
DR BioMuta; STAB2; -.
DR DMDM; 145559531; -.
DR EPD; Q8WWQ8; -.
DR jPOST; Q8WWQ8; -.
DR MassIVE; Q8WWQ8; -.
DR PaxDb; Q8WWQ8; -.
DR PeptideAtlas; Q8WWQ8; -.
DR PRIDE; Q8WWQ8; -.
DR ProteomicsDB; 74924; -.
DR Antibodypedia; 18052; 152 antibodies from 22 providers.
DR DNASU; 55576; -.
DR Ensembl; ENST00000388887.7; ENSP00000373539.2; ENSG00000136011.15.
DR GeneID; 55576; -.
DR KEGG; hsa:55576; -.
DR MANE-Select; ENST00000388887.7; ENSP00000373539.2; NM_017564.10; NP_060034.9.
DR UCSC; uc001tjw.4; human.
DR CTD; 55576; -.
DR DisGeNET; 55576; -.
DR GeneCards; STAB2; -.
DR HGNC; HGNC:18629; STAB2.
DR HPA; ENSG00000136011; Tissue enriched (lymphoid).
DR MIM; 608561; gene.
DR neXtProt; NX_Q8WWQ8; -.
DR OpenTargets; ENSG00000136011; -.
DR PharmGKB; PA38611; -.
DR VEuPathDB; HostDB:ENSG00000136011; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000156566; -.
DR HOGENOM; CLU_001035_0_0_1; -.
DR InParanoid; Q8WWQ8; -.
DR OMA; ENISNPM; -.
DR OrthoDB; 6428at2759; -.
DR PhylomeDB; Q8WWQ8; -.
DR TreeFam; TF331489; -.
DR PathwayCommons; Q8WWQ8; -.
DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
DR SignaLink; Q8WWQ8; -.
DR BioGRID-ORCS; 55576; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; STAB2; human.
DR GeneWiki; STAB2; -.
DR GenomeRNAi; 55576; -.
DR Pharos; Q8WWQ8; Tbio.
DR PRO; PR:Q8WWQ8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WWQ8; protein.
DR Bgee; ENSG00000136011; Expressed in spleen and 113 other tissues.
DR ExpressionAtlas; Q8WWQ8; baseline and differential.
DR Genevisible; Q8WWQ8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; NAS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB.
DR Gene3D; 2.30.180.10; -; 7.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR000538; Link_dom.
DR Pfam; PF12947; EGF_3; 9.
DR Pfam; PF02469; Fasciclin; 7.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 22.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00554; FAS1; 7.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF82153; SSF82153; 7.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 16.
DR PROSITE; PS50026; EGF_3; 21.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50213; FAS1; 7.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein;
KW Hyaluronic acid; Laminin EGF-like domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2551
FT /note="Stabilin-2"
FT /id="PRO_0000007712"
FT CHAIN 1136..2551
FT /note="190 kDa form stabilin-2"
FT /id="PRO_0000007713"
FT TOPO_DOM 20..2458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2459..2479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2480..2551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 108..148
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 156..193
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 195..236
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 237..276
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 322..362
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 371..505
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 515..652
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 736..776
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 826..866
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 867..909
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 910..952
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 953..992
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 994..1127
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1137..1265
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1343..1408
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1432..1470
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1471..1512
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1513..1554
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1555..1594
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1596..1724
FT /note="FAS1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1740..1881
FT /note="FAS1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1957..2022
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 2047..2081
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2082..2122
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2123..2165
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2198..2291
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 2311..2446
FT /note="FAS1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 2504..2514
FT /note="Interaction with TMSB4X"
FT /evidence="ECO:0000269|PubMed:18519035"
FT REGION 2512..2551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2512..2530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2533..2551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..126
FT /evidence="ECO:0000250"
FT DISULFID 120..136
FT /evidence="ECO:0000250"
FT DISULFID 138..147
FT /evidence="ECO:0000250"
FT DISULFID 160..171
FT /evidence="ECO:0000250"
FT DISULFID 164..181
FT /evidence="ECO:0000250"
FT DISULFID 183..192
FT /evidence="ECO:0000250"
FT DISULFID 199..210
FT /evidence="ECO:0000250"
FT DISULFID 204..222
FT /evidence="ECO:0000250"
FT DISULFID 224..235
FT /evidence="ECO:0000250"
FT DISULFID 241..252
FT /evidence="ECO:0000250"
FT DISULFID 246..262
FT /evidence="ECO:0000250"
FT DISULFID 264..275
FT /evidence="ECO:0000250"
FT DISULFID 326..338
FT /evidence="ECO:0000250"
FT DISULFID 332..348
FT /evidence="ECO:0000250"
FT DISULFID 350..361
FT /evidence="ECO:0000250"
FT DISULFID 740..754
FT /evidence="ECO:0000250"
FT DISULFID 748..764
FT /evidence="ECO:0000250"
FT DISULFID 766..775
FT /evidence="ECO:0000250"
FT DISULFID 830..843
FT /evidence="ECO:0000250"
FT DISULFID 837..852
FT /evidence="ECO:0000250"
FT DISULFID 854..865
FT /evidence="ECO:0000250"
FT DISULFID 871..885
FT /evidence="ECO:0000250"
FT DISULFID 879..895
FT /evidence="ECO:0000250"
FT DISULFID 897..908
FT /evidence="ECO:0000250"
FT DISULFID 914..928
FT /evidence="ECO:0000250"
FT DISULFID 922..938
FT /evidence="ECO:0000250"
FT DISULFID 940..951
FT /evidence="ECO:0000250"
FT DISULFID 957..970
FT /evidence="ECO:0000250"
FT DISULFID 964..980
FT /evidence="ECO:0000250"
FT DISULFID 1348..1362
FT /evidence="ECO:0000250"
FT DISULFID 1356..1372
FT /evidence="ECO:0000250"
FT DISULFID 1374..1383
FT /evidence="ECO:0000250"
FT DISULFID 1395..1406
FT /evidence="ECO:0000250"
FT DISULFID 1399..1416
FT /evidence="ECO:0000250"
FT DISULFID 1418..1427
FT /evidence="ECO:0000250"
FT DISULFID 1436..1446
FT /evidence="ECO:0000250"
FT DISULFID 1440..1456
FT /evidence="ECO:0000250"
FT DISULFID 1458..1469
FT /evidence="ECO:0000250"
FT DISULFID 1475..1488
FT /evidence="ECO:0000250"
FT DISULFID 1482..1498
FT /evidence="ECO:0000250"
FT DISULFID 1500..1511
FT /evidence="ECO:0000250"
FT DISULFID 1517..1530
FT /evidence="ECO:0000250"
FT DISULFID 1524..1540
FT /evidence="ECO:0000250"
FT DISULFID 1542..1553
FT /evidence="ECO:0000250"
FT DISULFID 1559..1572
FT /evidence="ECO:0000250"
FT DISULFID 1566..1582
FT /evidence="ECO:0000250"
FT DISULFID 1962..1976
FT /evidence="ECO:0000250"
FT DISULFID 1970..1986
FT /evidence="ECO:0000250"
FT DISULFID 1988..1997
FT /evidence="ECO:0000250"
FT DISULFID 2009..2020
FT /evidence="ECO:0000250"
FT DISULFID 2014..2030
FT /evidence="ECO:0000250"
FT DISULFID 2032..2041
FT /evidence="ECO:0000250"
FT DISULFID 2051..2061
FT /evidence="ECO:0000250"
FT DISULFID 2055..2067
FT /evidence="ECO:0000250"
FT DISULFID 2069..2080
FT /evidence="ECO:0000250"
FT DISULFID 2086..2099
FT /evidence="ECO:0000250"
FT DISULFID 2093..2108
FT /evidence="ECO:0000250"
FT DISULFID 2110..2121
FT /evidence="ECO:0000250"
FT DISULFID 2127..2141
FT /evidence="ECO:0000250"
FT DISULFID 2135..2151
FT /evidence="ECO:0000250"
FT DISULFID 2153..2164
FT /evidence="ECO:0000250"
FT DISULFID 2220..2289
FT /evidence="ECO:0000250"
FT DISULFID 2244..2265
FT /evidence="ECO:0000250"
FT VARIANT 110
FT /note="I -> V (in dbSNP:rs17034186)"
FT /id="VAR_048995"
FT VARIANT 306
FT /note="E -> K (in dbSNP:rs12319476)"
FT /id="VAR_048996"
FT VARIANT 510
FT /note="P -> H (in dbSNP:rs1609860)"
FT /evidence="ECO:0000269|PubMed:11829752,
FT ECO:0000269|PubMed:12077138"
FT /id="VAR_019541"
FT VARIANT 787
FT /note="R -> Q (in dbSNP:rs17034336)"
FT /id="VAR_048997"
FT VARIANT 881
FT /note="R -> H (in dbSNP:rs7973658)"
FT /id="VAR_048998"
FT VARIANT 1736
FT /note="N -> T (in dbSNP:rs17034433)"
FT /id="VAR_048999"
FT VARIANT 2039
FT /note="P -> T (in dbSNP:rs7306642)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_049000"
FT VARIANT 2401
FT /note="L -> V (in dbSNP:rs2271637)"
FT /evidence="ECO:0000269|Ref.5, ECO:0000269|Ref.7"
FT /id="VAR_049001"
FT VARIANT 2519
FT /note="Y -> S (in dbSNP:rs3751197)"
FT /id="VAR_049002"
FT CONFLICT 67
FT /note="G -> R (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="D -> A (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="K -> N (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT CONFLICT 1136
FT /note="S -> L (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151
FT /note="S -> P (in Ref. 1; CAC82105)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="D -> A (in Ref. 1; CAC82105)"
FT /evidence="ECO:0000305"
FT CONFLICT 1522
FT /note="G -> C (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT CONFLICT 1557
FT /note="N -> Y (in Ref. 6; AAO39681)"
FT /evidence="ECO:0000305"
FT CONFLICT 1599..1600
FT /note="IY -> HE (in Ref. 7; AAF82398)"
FT /evidence="ECO:0000305"
FT CONFLICT 1854
FT /note="F -> S (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT CONFLICT 2249
FT /note="L -> V (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT CONFLICT 2253
FT /note="R -> G (in Ref. 5; BAD18723)"
FT /evidence="ECO:0000305"
FT HELIX 2314..2318
FT /evidence="ECO:0007829|PDB:5N86"
FT HELIX 2322..2324
FT /evidence="ECO:0007829|PDB:5N86"
FT HELIX 2325..2335
FT /evidence="ECO:0007829|PDB:5N86"
FT HELIX 2339..2348
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2355..2360
FT /evidence="ECO:0007829|PDB:5N86"
FT TURN 2362..2364
FT /evidence="ECO:0007829|PDB:5N86"
FT HELIX 2373..2377
FT /evidence="ECO:0007829|PDB:5N86"
FT HELIX 2388..2390
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2396..2399
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2404..2410
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2415..2417
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2419..2422
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2425..2434
FT /evidence="ECO:0007829|PDB:5N86"
FT STRAND 2437..2444
FT /evidence="ECO:0007829|PDB:5N86"
SQ SEQUENCE 2551 AA; 276988 MW; 3ACB6A6C3CB80044 CRC64;
MMLQHLVIFC LGLVVQNFCS PAETTGQARR CDRKSLLTIR TECRSCALNL GVKCPDGYTM
ITSGSVGVRD CRYTFEVRTY SLSLPGCRHI CRKDYLQPRC CPGRWGPDCI ECPGGAGSPC
NGRGSCAEGM EGNGTCSCQE GFGGTACETC ADDNLFGPSC SSVCNCVHGV CNSGLDGDGT
CECYSAYTGP KCDKPIPECA ALLCPENSRC SPSTEDENKL ECKCLPNYRG DGKYCDPINP
CLRKICHPHA HCTYLGPNRH SCTCQEGYRG DGQVCLPVDP CQINFGNCPT KSTVCKYDGP
GQSHCECKEH YQNFVPGVGC SMTDICKSDN PCHRNANCTT VAPGRTECIC QKGYVGDGLT
CYGNIMERLR ELNTEPRGKW QGRLTSFISL LDKAYAWPLS KLGPFTVLLP TDKGLKGFNV
NELLVDNKAA QYFVKLHIIA GQMNIEYMNN TDMFYTLTGK SGEIFNSDKD NQIKLKLHGG
KKKVKIIQGD IIASNGLLHI LDRAMDKLEP TFESNNEQTI MTMLQPRYSK FRSLLEETNL
GHALDEDGVG GPYTIFVPNN EALNNMKDGT LDYLLSPEGS RKLLELVRYH IVPFTQLEVA
TLISTPHIRS MANQLIQFNT TDNGQILAND VAMEEIEITA KNGRIYTLTG VLIPPSIVPI
LPHRCDETKR EMKLGTCVSC SLVYWSRCPA NSEPTALFTH RCVYSGRFGS LKSGCARYCN
ATVKIPKCCK GFYGPDCNQC PGGFSNPCSG NGQCADSLGG NGTCICEEGF QGSQCQFCSD
PNKYGPRCNK KCLCVHGTCN NRIDSDGACL TGTCRDGSAG RLCDKQTSAC GPYVQFCHIH
ATCEYSNGTA SCICKAGYEG DGTLCSEMDP CTGLTPGGCS RNAECIKTGT GTHTCVCQQG
WTGNGRDCSE INNCLLPSAG GCHDNASCLY VGPGQNECEC KKGFRGNGID CEPITSCLEQ
TGKCHPLASC QSTSSGVWSC VCQEGYEGDG FLCYGNAAVE LSFLSEAAIF NRWINNASLQ
PTLSATSNLT VLVPSQQATE DMDQDEKSFW LSQSNIPALI KYHMLLGTYR VADLQTLSSS
DMLATSLQGN FLHLAKVDGN ITIEGASIVD GDNAATNGVI HIINKVLVPQ RRLTGSLPNL
LMRLEQMPDY SIFRGYIIQY NLANAIEAAD AYTVFAPNNN AIENYIREKK VLSLEEDVLR
YHVVLEEKLL KNDLHNGMHR ETMLGFSYFL SFFLHNDQLY VNEAPINYTN VATDKGVIHG
LGKVLEIQKN RCDNNDTTII RGRCRTCSSE LTCPFGTKSL GNEKRRCIYT SYFMGRRTLF
IGCQPKCVRT VITRECCAGF FGPQCQPCPG NAQNVCFGNG ICLDGVNGTG VCECGEGFSG
TACETCTEGK YGIHCDQACS CVHGRCNQGP LGDGSCDCDV GWRGVHCDNA TTEDNCNGTC
HTSANCLTNS DGTASCKCAA GFQGNGTICT AINACEISNG GCSAKADCKR TTPGRRVCTC
KAGYTGDGIV CLEINPCLEN HGGCDKNAEC TQTGPNQAAC NCLPAYTGDG KVCTLINVCL
TKNGGCSEFA ICNHTGQVER TCTCKPNYIG DGFTCRGSIY QELPKNPKTS QYFFQLQEHF
VKDLVGPGPF TVFAPLSAAF DEEARVKDWD KYGLMPQVLR YHVVACHQLL LENLKLISNA
TSLQGEPIVI SVSQSTVYIN NKAKIISSDI ISTNGIVHII DKLLSPKNLL ITPKDNSGRI
LQNLTTLATN NGYIKFSNLI QDSGLLSVIT DPIHTPVTLF WPTDQALHAL PAEQQDFLFN
QDNKDKLKEY LKFHVIRDAK VLAVDLPTST AWKTLQGSEL SVKCGAGRDI GDLFLNGQTC
RIVQRELLFD LGVAYGIDCL LIDPTLGGRC DTFTTFDASG ECGSCVNTPS CPRWSKPKGV
KQKCLYNLPF KRNLEGCRER CSLVIQIPRC CKGYFGRDCQ ACPGGPDAPC NNRGVCLDQY
SATGECKCNT GFNGTACEMC WPGRFGPDCL PCGCSDHGQC DDGITGSGQC LCETGWTGPS
CDTQAVLPAV CTPPCSAHAT CKENNTCECN LDYEGDGITC TVVDFCKQDN GGCAKVARCS
QKGTKVSCSC QKGYKGDGHS CTEIDPCADG LNGGCHEHAT CKMTGPGKHK CECKSHYVGD
GLNCEPEQLP IDRCLQDNGQ CHADAKCVDL HFQDTTVGVF HLRSPLGQYK LTFDKAREAC
ANEAATMATY NQLSYAQKAK YHLCSAGWLE TGRVAYPTAF ASQNCGSGVV GIVDYGPRPN
KSEMWDVFCY RMKDVNCTCK VGYVGDGFSC SGNLLQVLMS FPSLTNFLTE VLAYSNSSAR
GRAFLEHLTD LSIRGTLFVP QNSGLGENET LSGRDIEHHL ANVSMFFYND LVNGTTLQTR
LGSKLLITAS QDPLQPTETR FVDGRAILQW DIFASNGIIH VISRPLKAPP APVTLTHTGL
GAGIFFAIIL VTGAVALAAY SYFRINRRTI GFQHFESEED INVAALGKQQ PENISNPLYE
STTSAPPEPS YDPFTDSEER QLEGNDPLRT L
